ID   G8SL82_ACTS5            Unreviewed;       387 AA.
AC   G8SL82;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Methionine-gamma-lyase {ECO:0000313|EMBL:AEV81935.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:AEV81935.1};
GN   Name=megL {ECO:0000313|EMBL:AEV81935.1};
GN   OrderedLocusNames=ACPL_1038 {ECO:0000313|EMBL:AEV81935.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV81935.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CP003170; AEV81935.1; -; Genomic_DNA.
DR   RefSeq; WP_014688008.1; NZ_LT827010.1.
DR   AlphaFoldDB; G8SL82; -.
DR   STRING; 134676.ACPL_1038; -.
DR   KEGG; ase:ACPL_1038; -.
DR   PATRIC; fig|134676.3.peg.930; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_11; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000005440; Chromosome.
DR   GO; GO:0018826; F:methionine gamma-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:AEV81935.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005440}.
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   387 AA;  41189 MW;  D76DFACD1E8935EF CRC64;
     MHPETRLIHL KAPVPQGSTP LAVPIYQTSS FAFDDPELIA DGLHHPDRAY AYSRFANPTV
     RALENAITDL EGGAAAIATS SGMGAITLLL HGLLSAGDHV IVQRDVYGGT HAQLGDLAAR
     FGIEVTRIGG HDPAELRAAL TPRTRVLYLE TIANPTGHVS DLPTLAPIAR DAGVLTVVDN
     TFASPIFCRP IEHGADVVVH SVTKFLGGHS DVTGGLAVFA DRALYERVWE QSVEFGATAD
     PFAAWLTLRG LHTLGLRMDR HAANTARVAT WLAAHPAVEA VRWTGDPSHP SHAVASRFVQ
     GFTGAFCFDL DGGHDAGVRL MSRLTVIRAA ASLGSTQSLI LHPASTTHRQ LTPDQLRESH
     LSPGTVRIAI GIEHPDDLVA DLEQALG
//